Reviewed, UniProtKB/Swiss-Prot Q9D9M5 (PHOP2_MOUSE)

Names and origin

Protein names

Recommended name:
    Pyridoxal phosphate phosphatase PHOSPHO2
    EC=3.1.3.74

Gene names

Name:

Phospho2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Phosphatase that has high activity toward pyridoxal 5'-phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate By similarity.
Catalytic activity	Pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.
Cofactor	Magnesium By similarity.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. PHOSPHO family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding Pyridoxal phosphate
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyridoxal phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 241	241	Pyridoxal phosphate phosphatase PHOSPHO2		PRO_0000068834
Sites
	Active site	8	1	Nucleophile By similarity
	Active site	10	1	Proton donor By similarity
	Metal binding	8	1	Magnesium By similarity
	Metal binding	10	1	Magnesium By similarity
	Metal binding	179	1	Magnesium By similarity
	Binding site	19	1	Substrate By similarity
	Binding site	99	1	Substrate By similarity
Experimental info
	Sequence conflict	186	1	P → Q in BAE21125. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9D9M5-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 9E0036C310AD26BE	FASTA	241	27,563
	10 20 30 40 50 60 MKVLLVFDFD NTIIDDNSDT WIVQCAPDKK LPIELQDSYQ KGLWTEFMGR VFKYLRDEGV 70 80 90 100 110 120 KADELKRAVT SLPFTSGMIE LLSFLRMNKD RFDCIIISDS NSIFIDWVLE AAAFHDVFDH 130 140 150 160 170 180 VFTNPASFDS SGRLTVKNYH AHSCTRCPKN LCKNTVLGEF IDKQLQKGVR YTRIVYIGDG 190 200 210 220 230 240 GNDVCPVTFL KKNDVAMPRE GYTLHRTLAK MSQNLEPMES SIVVWSSGVE IISHLQFLIK M

References

[1]

"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head and Testis.

[2]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK006724 mRNA. Translation: BAB24714.1. AK132362 mRNA. Translation: BAE21125.1. AK159551 mRNA. Translation: BAE35176.1. BC025612 mRNA. Translation: AAH25612.1. BC031523 mRNA. Translation: AAH31523.1.
IPI	IPI00112884.
RefSeq	NP_082797.1.
UniGene	Mm.9621
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9D9M5.
Genome annotation databases
Ensembl	ENSMUSG00000027088. Mus musculus. [Contig view]
GeneID	73373.
KEGG	mmu:73373.
Organism-specific databases
MGI	MGI:1920623. Phospho2.
Phylogenomic databases
HOGENOM	Q9D9M5.
HOVERGEN	Q9D9M5.
OMA	Q9D9M5. NDVAMPR.
Enzyme and pathway databases
BRENDA	3.1.3.74. 244.
Gene expression databases
ArrayExpress	Q9D9M5.
Bgee	Q9D9M5.
CleanEx	MM_PHOSPHO2.
GermOnline	ENSMUSG00000027088. Mus musculus.
Family and domain databases
InterPro	IPR006383. HAD-SF_hydro_IB_PSP-like. IPR006384. PyrdxlP_Pase-rel. IPR016965. PyrdxlP_Pase_PHOSPHO2. [Graphical view]
Pfam	PF06888. Put_Phosphatase. 1 hit. [Graphical view]
PIRSF	PIRSF031051. PyrdxlP_Pase_PHOSPHO2. 1 hit.
TIGRFAMs	TIGR01489. DKMTPPase-SF. 1 hit. TIGR01488. HAD-SF-IB. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	338097.
SOURCE	Search...

Entry information

Entry name

PHOP2_MOUSE

Accession

Primary (citable) accession number: Q9D9M5
Secondary accession number(s): Q3V1M5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)